Vinothkumar, K.R. & Henderson, R. (2010).
Structures of Membrane Proteins.
Quarterly Reviews of Biophysics, 43, 65-158.
Henderson, R., Chen, S., Chen, J.Z., Grigorieff, N., Passmore, L.A., Ciccarelli, L., Rubinstein, J.L., Crowther, R.A., Stewart, P.L. & Rosenthal. P.B. (2011)
Tilt-pair analysis of images from a range of different specimens in single particle electron cryomicroscopy.
J. Mol. Biol. 413, 1028-1046.
Glaeser, R.M., McMullan, G., Henderson, R. & Faruqi, A.R. (2011)
Images of paraffin monolayer crystals with perfect contrast: Minimization of beam-induced specimen motion.
Ultramicroscopy 111, 90-100.
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Group Members
- Wasi Faruqi
- Jude Short (Smith)
- Greg McMullan
- Shaoxia Chen
- Vinothkumar Kutti Ragunath
- Daria Slowik
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| We aim to determine the atomic structure of interesting or important membrane proteins and membrane protein complexes. Although much can be done using existing methods and approaches such as X-ray crystallography of 3D crystals or electron crystallography of 2D crystals, there are still many structures that have resisted our best efforts to crystallise them even when significant amounts of pure material have been obtained. There are two main problems.
First, many membrane proteins, including most G-protein-coupled receptors, are relatively unstable after purification in detergent: for this class of membrane proteins, Chris Tate and his colleagues in the LMB have recently developed the method of conformational stabilisation (Serrano- Vega et al (2008) PNAS, 105, 877-882) by combining a number of thermostabilising mutants to create much more stable molecules. This has made it possible to tackle structures that were practically impossible previously.
A second problem is the need to make well-ordered crystals that diffract to high resolution. If the resolution of single particle electron cryomicroscopy could be improved, then crystallisation would no longer be needed to obtain atomic structures. We are therefore working to improve the imaging methods, the computer programs for image processing, and the efficiency of electron detectors, with the goal of realising the potential of electron cryomicroscopy for analysis of single particle structure at atomic resolution.
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Collage of membrane protein structures determined in the LMB:(left to right) acetylcholine receptor (Unwin), rhodopsin (Li & Schertler),?-adrenergic receptor (Schertler), bacteriorhodopsin (Henderson),ATP-synthase (Stock & Walker) |
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Group Leaders 
